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M602474200v1
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Papers In Press, published online ahead of print September 15, 2006
J. Biol. Chem, 10.1074/jbc.M602474200
Submitted on March 16, 2006
Revised on September 14, 2006
Accepted on September 15, 2006

alpha actinin 4 potentiates MEF2 transcription activity by antagonizing histone deacetylase 7

Sharmistha Chakraborty, Erin L. Reineke, Minh Lam, Xiaofang Li, Yu Liu, Chengzhuo Gao, Simran Khurana, and Hung-Ying Kao

Department of Biochemistry, Case Western Reserve University, Cleveland, OH 44106

Corresponding Author: hxk43{at}po.cwru.edu

Histone deacetylase 7 (HDAC7) is a member of class IIa HDACs that regulate MEF2-mediated transcription and participate in multiple cellular processes such as T cell apoptosis. We have identified a actinin 1 and 4 as class IIa HDAC interacting proteins. The interaction domains are mapped to C-terminus of a actinin 4 and amino acids 72-172 of HDAC7. A point mutation in HDAC7 that disrupts its association with MEF2A also disrupts its association with a actinin 4, indicating that MEF2A and a actinin 4 binding sites are largely overlapping. We have also isolated a novel splice variant of a actinin 4 that is predominantly localized in the nucleus, a pattern distinct from the full-length a actinin 4, which is primarily distributed in the cytoplasm and plasma membrane. Using siRNA, chromatin immunoprecipitation, and transient transfection assays, we show that a actinin 4 potentiates expression of TAF55, a putative MEF2 target gene. Loss of MEF2A interaction correlates with loss of the ability of a actinin 4 to potentaite TAF55 promoter activity. Ectopic expression of a actinin 4, but not the mutant defective in MEF2A association, leads to disruption of HDAC7:MEF2A association and enhancement of MEF2-mediated transcription. Taken together, we have identified a novel mechanism by which HDAC7 activity is negatively regulated and uncovered a previously unknown function of a actinin 4.


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